FMO DATABASE

FMODB ID: LQ9N9

Calculation Name: 1K66-A-Xray547

Preferred Name:

Target Type:

Ligand Name: beta-mercaptoethanol

Ligand 3-letter code: BME

Ligand of Interest (LOI):

Structure Source: PDB

PDB ID: 1K66

Chain ID: A

ChEMBL ID:

UniProt ID: Q8RTM8

Base Structure: X-ray

Registration Date: 2025-10-03

Reference: Sci Data 11, 1164 (2024).

DOI: https://doi.org/10.1038/s41597-024-03999-2

Apendix: None

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Homology Modeling
Water	No
Procedure	Manual calculation
Remarks	ac.sh, 23 2024 Oct; Missing atoms/residues were imported from a 100% homology model, which was constructed by MOE.

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	149
LigandResidueName
LigandFragmentNumber	0
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 23 (BINDS Ver. 1) / 20230922

Total energy (hartree)

FMO2-HF: Electronic energy	-1449553.104279
FMO2-HF: Nuclear repulsion	1390655.10401
FMO2-HF: Total energy	-58898.000269
FMO2-MP2: Total energy	-59069.577162

3D Structure Molmil

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:1:ALA)

Summations of interaction energy for fragment #1(A:1:ALA)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-203.214	-197.588	5.906	-6.084	-5.447	-0.059

Interaction energy analysis for fragmet #1(A:1:ALA)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.780 / q_NPA : 0.883

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	3	GLY	0	0.127	0.076	3.850	1.898	3.559	-0.019	-0.819	-0.824	-0.003
30	A	30	GLY	0	-0.059	-0.022	2.562	-19.046	-17.396	0.459	-1.122	-0.987	-0.010
31	A	31	VAL	0	-0.003	-0.010	2.222	-20.795	-19.064	4.765	-3.749	-2.747	-0.040
32	A	32	VAL	0	-0.045	-0.025	2.342	2.359	2.953	0.702	-0.391	-0.904	-0.006
33	A	33	ASN	0	0.007	0.007	5.100	0.708	0.698	-0.001	-0.003	0.015	0.000
4	A	4	ASN	0	-0.010	0.001	5.746	-2.427	-2.427	0.000	0.000	0.000	0.000
5	A	5	ALA	0	0.021	0.009	7.195	2.003	2.003	0.000	0.000	0.000	0.000
6	A	6	THR	0	-0.075	-0.061	8.604	2.378	2.378	0.000	0.000	0.000	0.000
7	A	7	GLN	0	0.042	0.017	11.059	0.134	0.134	0.000	0.000	0.000	0.000
8	A	8	PRO	0	0.010	0.008	11.801	-1.672	-1.672	0.000	0.000	0.000	0.000
9	A	9	LEU	0	-0.013	0.007	12.749	0.328	0.328	0.000	0.000	0.000	0.000
10	A	10	LEU	0	-0.012	-0.002	14.669	-0.040	-0.040	0.000	0.000	0.000	0.000
11	A	11	VAL	0	-0.016	-0.015	16.245	0.056	0.056	0.000	0.000	0.000	0.000
12	A	12	VAL	0	-0.008	-0.007	19.199	0.340	0.340	0.000	0.000	0.000	0.000
13	A	13	GLU	-1	-0.788	-0.892	20.970	-13.281	-13.281	0.000	0.000	0.000	0.000
14	A	14	ASP	-1	-0.855	-0.931	23.465	-11.183	-11.183	0.000	0.000	0.000	0.000
15	A	15	SER	0	-0.007	0.012	24.317	0.188	0.188	0.000	0.000	0.000	0.000
16	A	16	ASP	-1	-0.817	-0.902	22.908	-12.921	-12.921	0.000	0.000	0.000	0.000
17	A	17	GLU	-1	-0.921	-0.973	21.557	-13.979	-13.979	0.000	0.000	0.000	0.000
18	A	18	ASP	-1	-0.834	-0.898	20.679	-13.791	-13.791	0.000	0.000	0.000	0.000
19	A	19	PHE	0	0.025	0.004	16.605	-1.128	-1.128	0.000	0.000	0.000	0.000
20	A	20	SER	0	-0.010	0.005	16.879	-1.547	-1.547	0.000	0.000	0.000	0.000
21	A	21	THR	0	-0.031	-0.025	16.500	-1.114	-1.114	0.000	0.000	0.000	0.000
22	A	22	PHE	0	0.023	0.006	14.204	-1.575	-1.575	0.000	0.000	0.000	0.000
23	A	23	GLN	0	0.019	0.008	12.685	-1.190	-1.190	0.000	0.000	0.000	0.000
24	A	24	ARG	1	0.884	0.936	11.249	15.358	15.358	0.000	0.000	0.000	0.000
25	A	25	LEU	0	-0.015	0.001	10.843	-2.287	-2.287	0.000	0.000	0.000	0.000
26	A	26	LEU	0	0.035	0.011	8.439	-3.173	-3.173	0.000	0.000	0.000	0.000
27	A	27	GLN	0	-0.028	-0.016	6.641	-4.566	-4.566	0.000	0.000	0.000	0.000
28	A	28	ARG	1	0.846	0.933	6.667	26.607	26.607	0.000	0.000	0.000	0.000
29	A	29	GLU	-1	-0.853	-0.913	5.547	-38.373	-38.373	0.000	0.000	0.000	0.000
34	A	34	PRO	0	-0.029	0.001	8.620	0.001	0.001	0.000	0.000	0.000	0.000
35	A	35	ILE	0	0.006	-0.002	10.487	1.081	1.081	0.000	0.000	0.000	0.000
36	A	36	TYR	0	0.011	0.007	13.517	0.776	0.776	0.000	0.000	0.000	0.000
37	A	37	ARG	1	0.771	0.862	17.245	13.236	13.236	0.000	0.000	0.000	0.000
38	A	38	CYS	0	-0.057	-0.008	20.154	0.554	0.554	0.000	0.000	0.000	0.000
39	A	39	ILE	0	0.016	0.008	23.823	-0.228	-0.228	0.000	0.000	0.000	0.000
40	A	40	THR	0	0.007	-0.007	26.351	0.115	0.115	0.000	0.000	0.000	0.000
41	A	41	GLY	0	0.081	0.032	28.174	-0.365	-0.365	0.000	0.000	0.000	0.000
42	A	42	ASP	-1	-0.825	-0.899	29.853	-9.346	-9.346	0.000	0.000	0.000	0.000
43	A	43	GLN	0	0.025	0.012	26.886	-0.349	-0.349	0.000	0.000	0.000	0.000
44	A	44	ALA	0	0.034	0.009	25.481	-0.251	-0.251	0.000	0.000	0.000	0.000
45	A	45	LEU	0	0.017	0.007	26.454	-0.210	-0.210	0.000	0.000	0.000	0.000
46	A	46	ASP	-1	-0.751	-0.875	29.242	-9.862	-9.862	0.000	0.000	0.000	0.000
47	A	47	PHE	0	0.008	-0.007	19.730	-0.036	-0.036	0.000	0.000	0.000	0.000
48	A	48	LEU	0	-0.038	-0.023	22.575	-0.234	-0.234	0.000	0.000	0.000	0.000
49	A	49	TYR	0	-0.051	-0.025	25.810	-0.070	-0.070	0.000	0.000	0.000	0.000
50	A	50	GLN	0	-0.097	-0.038	25.294	0.282	0.282	0.000	0.000	0.000	0.000
51	A	51	THR	0	-0.024	-0.006	28.396	0.205	0.205	0.000	0.000	0.000	0.000
52	A	52	GLY	0	-0.005	0.007	30.292	0.291	0.291	0.000	0.000	0.000	0.000
53	A	53	SER	0	-0.092	-0.051	31.300	0.278	0.278	0.000	0.000	0.000	0.000
54	A	54	TYR	0	-0.114	-0.061	30.518	0.220	0.220	0.000	0.000	0.000	0.000
55	A	55	CYS	0	-0.073	-0.027	25.917	-0.231	-0.231	0.000	0.000	0.000	0.000
56	A	56	ASN	0	-0.006	-0.004	26.728	-0.117	-0.117	0.000	0.000	0.000	0.000
57	A	57	PRO	0	0.054	0.029	25.780	-0.421	-0.421	0.000	0.000	0.000	0.000
58	A	58	ASP	-1	-0.893	-0.949	25.129	-10.937	-10.937	0.000	0.000	0.000	0.000
59	A	59	ILE	0	-0.094	-0.051	21.733	-0.498	-0.498	0.000	0.000	0.000	0.000
60	A	60	ALA	0	-0.008	0.004	21.169	-0.549	-0.549	0.000	0.000	0.000	0.000
61	A	61	PRO	0	-0.041	-0.002	17.705	0.255	0.255	0.000	0.000	0.000	0.000
62	A	62	ARG	1	0.926	0.949	19.702	11.957	11.957	0.000	0.000	0.000	0.000
63	A	63	PRO	0	-0.041	-0.014	17.177	-0.662	-0.662	0.000	0.000	0.000	0.000
64	A	64	ALA	0	0.030	0.007	14.947	0.577	0.577	0.000	0.000	0.000	0.000
65	A	65	VAL	0	-0.039	-0.017	15.190	0.107	0.107	0.000	0.000	0.000	0.000
66	A	66	ILE	0	0.025	0.013	17.398	-0.256	-0.256	0.000	0.000	0.000	0.000
67	A	67	LEU	0	-0.036	-0.011	16.678	-0.083	-0.083	0.000	0.000	0.000	0.000
68	A	68	LEU	0	0.002	0.001	19.833	0.134	0.134	0.000	0.000	0.000	0.000
69	A	69	ASP	-1	-0.676	-0.806	23.407	-11.490	-11.490	0.000	0.000	0.000	0.000
70	A	70	LEU	0	-0.008	-0.018	25.660	0.223	0.223	0.000	0.000	0.000	0.000
71	A	71	ASN	0	-0.061	-0.031	29.088	0.728	0.728	0.000	0.000	0.000	0.000
72	A	72	LEU	0	0.038	0.028	26.359	-0.365	-0.365	0.000	0.000	0.000	0.000
73	A	73	PRO	0	-0.038	-0.010	29.569	0.404	0.404	0.000	0.000	0.000	0.000
74	A	74	GLY	0	-0.009	-0.012	31.996	-0.206	-0.206	0.000	0.000	0.000	0.000
75	A	75	THR	0	-0.024	-0.033	32.983	0.188	0.188	0.000	0.000	0.000	0.000
76	A	76	ASP	-1	-0.791	-0.884	32.211	-9.691	-9.691	0.000	0.000	0.000	0.000
77	A	77	GLY	0	0.064	0.014	29.205	-0.083	-0.083	0.000	0.000	0.000	0.000
78	A	78	ARG	1	0.712	0.803	29.946	9.277	9.277	0.000	0.000	0.000	0.000
79	A	79	GLU	-1	-0.939	-0.962	32.620	-8.375	-8.375	0.000	0.000	0.000	0.000
80	A	80	VAL	0	-0.012	0.007	27.554	-0.036	-0.036	0.000	0.000	0.000	0.000
81	A	81	LEU	0	-0.030	-0.014	27.856	-0.118	-0.118	0.000	0.000	0.000	0.000
82	A	82	GLN	0	-0.039	-0.030	30.074	0.208	0.208	0.000	0.000	0.000	0.000
83	A	83	GLU	-1	-0.884	-0.943	32.254	-8.727	-8.727	0.000	0.000	0.000	0.000
84	A	84	ILE	0	-0.019	-0.009	26.371	-0.016	-0.016	0.000	0.000	0.000	0.000
85	A	85	LYS	1	0.816	0.905	26.221	11.438	11.438	0.000	0.000	0.000	0.000
86	A	86	GLN	0	-0.090	-0.043	31.247	0.353	0.353	0.000	0.000	0.000	0.000
87	A	87	ASP	-1	-0.802	-0.890	30.353	-9.805	-9.805	0.000	0.000	0.000	0.000
88	A	88	GLU	-1	-0.899	-0.963	31.021	-9.445	-9.445	0.000	0.000	0.000	0.000
89	A	89	VAL	0	-0.087	-0.043	26.629	-0.178	-0.178	0.000	0.000	0.000	0.000
90	A	90	LEU	0	0.020	-0.006	25.593	-0.502	-0.502	0.000	0.000	0.000	0.000
91	A	91	LYS	1	0.864	0.964	26.167	9.005	9.005	0.000	0.000	0.000	0.000
92	A	92	LYS	1	0.822	0.901	25.438	11.489	11.489	0.000	0.000	0.000	0.000
93	A	93	ILE	0	0.005	0.012	20.556	-0.479	-0.479	0.000	0.000	0.000	0.000
94	A	94	PRO	0	-0.059	-0.031	19.203	0.353	0.353	0.000	0.000	0.000	0.000
95	A	95	VAL	0	0.032	0.032	20.597	-0.528	-0.528	0.000	0.000	0.000	0.000
96	A	96	VAL	0	-0.014	-0.008	18.723	0.333	0.333	0.000	0.000	0.000	0.000
97	A	97	ILE	0	0.006	0.004	21.696	-0.033	-0.033	0.000	0.000	0.000	0.000
98	A	98	MET	0	-0.021	-0.023	18.706	-0.593	-0.593	0.000	0.000	0.000	0.000
99	A	99	THR	0	-0.012	-0.017	22.805	0.220	0.220	0.000	0.000	0.000	0.000
100	A	100	THR	0	0.005	0.007	25.933	-0.095	-0.095	0.000	0.000	0.000	0.000
101	A	101	SER	0	-0.063	-0.042	28.234	0.358	0.358	0.000	0.000	0.000	0.000
102	A	102	SER	0	0.047	0.019	29.920	-0.208	-0.208	0.000	0.000	0.000	0.000
103	A	103	ASN	0	0.001	0.002	31.728	0.235	0.235	0.000	0.000	0.000	0.000
104	A	104	PRO	0	0.057	0.018	34.075	-0.110	-0.110	0.000	0.000	0.000	0.000
105	A	105	LYS	1	0.918	0.975	35.704	7.764	7.764	0.000	0.000	0.000	0.000
106	A	106	ASP	-1	-0.691	-0.792	32.163	-9.363	-9.363	0.000	0.000	0.000	0.000
107	A	107	ILE	0	0.001	0.014	30.361	-0.197	-0.197	0.000	0.000	0.000	0.000
108	A	108	GLU	-1	-0.884	-0.957	32.224	-9.253	-9.253	0.000	0.000	0.000	0.000
109	A	109	ILE	0	-0.043	-0.007	34.436	0.089	0.089	0.000	0.000	0.000	0.000
110	A	110	CYS	0	-0.002	-0.009	29.407	-0.085	-0.085	0.000	0.000	0.000	0.000
111	A	111	TYR	0	0.015	-0.008	26.915	-0.407	-0.407	0.000	0.000	0.000	0.000
112	A	112	SER	0	-0.065	-0.038	31.462	0.087	0.087	0.000	0.000	0.000	0.000
113	A	113	TYR	0	-0.055	-0.021	32.099	0.147	0.147	0.000	0.000	0.000	0.000
114	A	114	SER	0	-0.044	-0.019	29.770	-0.212	-0.212	0.000	0.000	0.000	0.000
115	A	115	ILE	0	-0.026	-0.008	25.842	-0.294	-0.294	0.000	0.000	0.000	0.000
116	A	116	SER	0	-0.039	-0.017	21.797	0.324	0.324	0.000	0.000	0.000	0.000
117	A	117	SER	0	-0.028	-0.024	21.478	-0.339	-0.339	0.000	0.000	0.000	0.000
118	A	118	TYR	0	-0.004	-0.012	23.827	-0.078	-0.078	0.000	0.000	0.000	0.000
119	A	119	ILE	0	-0.046	-0.020	19.332	-0.047	-0.047	0.000	0.000	0.000	0.000
120	A	120	VAL	0	-0.008	-0.004	23.599	0.256	0.256	0.000	0.000	0.000	0.000
121	A	121	LYS	1	0.752	0.841	22.380	12.496	12.496	0.000	0.000	0.000	0.000
122	A	122	PRO	0	-0.050	-0.010	21.479	0.513	0.513	0.000	0.000	0.000	0.000
123	A	123	LEU	0	0.030	0.010	23.484	-0.206	-0.206	0.000	0.000	0.000	0.000
124	A	124	GLU	-1	-0.928	-0.964	24.167	-12.187	-12.187	0.000	0.000	0.000	0.000
125	A	125	ILE	0	0.039	0.004	18.946	-0.553	-0.553	0.000	0.000	0.000	0.000
126	A	126	ASP	-1	-0.935	-0.946	18.897	-16.174	-16.174	0.000	0.000	0.000	0.000
127	A	127	ARG	1	1.019	1.007	18.802	13.319	13.319	0.000	0.000	0.000	0.000
128	A	128	LEU	0	0.027	0.016	17.611	-0.491	-0.491	0.000	0.000	0.000	0.000
129	A	129	THR	0	-0.012	-0.016	13.780	-1.140	-1.140	0.000	0.000	0.000	0.000
130	A	130	GLU	-1	-0.924	-0.955	14.495	-20.333	-20.333	0.000	0.000	0.000	0.000
131	A	131	THR	0	-0.054	-0.040	15.839	-0.425	-0.425	0.000	0.000	0.000	0.000
132	A	132	VAL	0	0.007	0.002	11.880	-0.375	-0.375	0.000	0.000	0.000	0.000
133	A	133	GLN	0	-0.041	-0.038	10.316	0.122	0.122	0.000	0.000	0.000	0.000
134	A	134	THR	0	-0.048	-0.024	11.703	-1.373	-1.373	0.000	0.000	0.000	0.000
135	A	135	PHE	0	-0.011	-0.009	12.795	-0.324	-0.324	0.000	0.000	0.000	0.000
136	A	136	ILE	0	0.010	-0.001	7.341	-0.371	-0.371	0.000	0.000	0.000	0.000
137	A	137	LYS	1	0.956	0.975	9.578	26.867	26.867	0.000	0.000	0.000	0.000
138	A	138	TYR	0	-0.006	0.000	11.257	0.419	0.419	0.000	0.000	0.000	0.000
139	A	139	TRP	0	0.038	-0.009	13.844	0.629	0.629	0.000	0.000	0.000	0.000
140	A	140	LEU	0	-0.041	-0.018	9.102	0.398	0.398	0.000	0.000	0.000	0.000
141	A	141	ASP	-1	-0.988	-0.987	8.718	-37.129	-37.129	0.000	0.000	0.000	0.000
142	A	142	ILE	0	-0.033	-0.013	10.511	1.607	1.607	0.000	0.000	0.000	0.000
143	A	143	VAL	0	-0.038	-0.011	14.107	1.423	1.423	0.000	0.000	0.000	0.000
144	A	144	VAL	0	-0.027	-0.011	15.353	-0.760	-0.760	0.000	0.000	0.000	0.000
145	A	145	LEU	0	-0.022	-0.003	13.870	1.157	1.157	0.000	0.000	0.000	0.000
146	A	146	PRO	0	-0.017	-0.001	17.663	0.227	0.227	0.000	0.000	0.000	0.000
147	A	147	GLU	-1	-0.954	-0.985	18.770	-14.436	-14.436	0.000	0.000	0.000	0.000
148	A	148	MET	0	-0.067	-0.038	16.088	0.264	0.264	0.000	0.000	0.000	0.000
149	A	149	GLY	-1	-0.780	-0.866	19.639	-12.132	-12.132	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:1:ALA)